1fuk
From Proteopedia
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| - | [[Image:1fuk.jpg|left|200px]] | + | [[Image:1fuk.jpg|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF THE CARBOXY TERMINAL DOMAIN OF YEAST EIF4A''' | + | {{Structure |
| + | |PDB= 1fuk |SIZE=350|CAPTION= <scene name='initialview01'>1fuk</scene>, resolution 1.75Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF THE CARBOXY TERMINAL DOMAIN OF YEAST EIF4A''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1FUK is a [ | + | 1FUK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FUK OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase., Caruthers JM, Johnson ER, McKay DB, Proc Natl Acad Sci U S A. 2000 Nov 21;97(24):13080-5. PMID:[http:// | + | Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase., Caruthers JM, Johnson ER, McKay DB, Proc Natl Acad Sci U S A. 2000 Nov 21;97(24):13080-5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11087862 11087862] |
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: initiation factor 4a]] | [[Category: initiation factor 4a]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:14:10 2008'' |
Revision as of 09:14, 20 March 2008
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| , resolution 1.75Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF THE CARBOXY TERMINAL DOMAIN OF YEAST EIF4A
Overview
The eukaryotic translation initiation factor 4A (eIF4A) is a member of the DEA(D/H)-box RNA helicase family, a diverse group of proteins that couples an ATPase activity to RNA binding and unwinding. Previous work has provided the structure of the amino-terminal, ATP-binding domain of eIF4A. Extending those results, we have solved the structure of the carboxyl-terminal domain of eIF4A with data to 1.75 A resolution; it has a parallel alpha-beta topology that superimposes, with minor variations, on the structures and conserved motifs of the equivalent domain in other, distantly related helicases. Using data to 2.8 A resolution and molecular replacement with the refined model of the carboxyl-terminal domain, we have completed the structure of full-length eIF4A; it is a "dumbbell" structure consisting of two compact domains connected by an extended linker. By using the structures of other helicases as a template, compact structures can be modeled for eIF4A that suggest (i) helicase motif IV binds RNA; (ii) Arg-298, which is conserved in the DEA(D/H)-box RNA helicase family but is absent from many other helicases, also binds RNA; and (iii) motifs V and VI "link" the carboxyl-terminal domain to the amino-terminal domain through interactions with ATP and the DEA(D/H) motif, providing a mechanism for coupling ATP binding and hydrolysis with conformational changes that modulate RNA binding.
About this Structure
1FUK is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase., Caruthers JM, Johnson ER, McKay DB, Proc Natl Acad Sci U S A. 2000 Nov 21;97(24):13080-5. PMID:11087862
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